Q6HL37 (HIS81_BACHK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidinol-phosphate aminotransferase 1
EC=2.6.1.9

Alternative name(s):
Imidazole acetol-phosphate transaminase 1

Gene names

Name:	hisC1
Ordered Locus Names:	BT9727_1400

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023
Cofactor	Pyridoxal phosphate By similarity. HAMAP MF_01023
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023
Subunit structure	Homodimer By similarity. HAMAP MF_01023
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-phenylalanine:2-oxoglutarate aminotransferase activity Inferred from electronic annotation. Source: EC histidinol-phosphate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 370	370	Histidinol-phosphate aminotransferase 1 HAMAP MF_01023		PRO_0000153310
Amino acid modifications
	Modified residue	222	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6HL37 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: B06A624B5EDC93F1	FASTA	370	41,603
	10 20 30 40 50 60 MRVKEQLLTL RAYVPGKNIE EVKREYGLSK IVKLASNENP FGCSARVTEA LTSLASQYAL 70 80 90 100 110 120 YPDGHAFELR TKVAKHLGVK AEQLLFGSGL DEVIQMISRA LLHEGTNVVM ANPTFSQYHH 130 140 150 160 170 180 HAVIEGAEVR EVSLKDGIHD LDAMLQQVDD QTKIVWICNP NNPTGTYVEK QKLLSFLESV 190 200 210 220 230 240 PKSALVIMDE AYYEYAGAED YPQTLPLLEK YENLMVLRTF SKAYGLAAFR IGYAVGNTEL 250 260 270 280 290 300 IGQLEVARLP FNTSTVAQSV ALAALEDQAF LQECVKKNEE GLHQYYAFCK EYNVFYYPSQ 310 320 330 340 350 360 TNFIFLKLGI PGNEAFERLM KKGYIVRSGA AFGIDDGIRI TVGLKEENDE IIELLKELVN 370 EQVQKEETYS

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT59458.1.
RefSeq	YP_035734.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HL37.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000072751; EBBACP00000070837; EBBACG00000072742.
GeneID	2855566.
GenomeReviews	Gene locus BT9727_1400 in contig AE017355_GR.
KEGG	btk:BT9727_1400.
NMPDR	fig|281309.1.peg.1374.
PATRIC	18983485. VBIBacThu119411_1472.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000000787.
HOGENOM	HBG646350.
OMA	ENPLGMP.
ProtClustDB	PRK03158.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_1400-MONOMER.
Family and domain databases
HAMAP	MF_01023. HisC_aminotrans_2. [Tree]
InterPro	IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR005861. HisP_aminotrans. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
KO	K00817.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01141. HisC. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS81_BACHK

Accession

Primary (citable) accession number: Q6HL37

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program